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The pitch of the alpha-helix (the vertical distance between consecutive turns of the helix) is 5.4 Å (0.54 nm), which is the product of 1.5 and 3.6. The most important thing is that the N-H group of one amino acid forms a hydrogen bond with the C=O group of the amino acid four residues earlier; this repeated i + 4 → i hydrogen bonding is the ...
Alpha-keratin, or α-keratin, is a type of keratin found in mammalian vertebrates. This protein is the primary component in hairs , horns , claws , nails and the epidermis layer of the skin . α-keratin is a fibrous structural protein , meaning it is made up of amino acids that form a repeating secondary structure.
The loops connecting the beta strands and alpha helix can vary in length and often binds ligands. Beta-alpha-beta helices can be either left-handed or right-handed. When viewed from the N-terminal side of the beta strands, so that one strand is on top of the other, a left-handed beta-alpha-beta motif has the alpha helix on the left side of the ...
G = 3-turn helix (3 10 helix). Min length 3 residues. H = 4-turn helix . Minimum length 4 residues. I = 5-turn helix . Minimum length 5 residues. T = hydrogen bonded turn (3, 4 or 5 turn) E = extended strand in parallel and/or anti-parallel β-sheet conformation. Min length 2 residues.
Helix-loop-helix Consists of alpha helices bound by a looping stretch of amino acids. This motif is seen in transcription factors. Zinc finger Two beta strands with an alpha helix end folded over to bind a zinc ion. Important in DNA binding proteins. Helix-turn-helix
An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns). The alignment of the H-bonds ...
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Hydrophobicity scales can also be obtained by calculating the solvent accessible surface areas for amino acid residues in the expended polypeptide chain [22] or in alpha-helix and multiplying the surface areas by the empirical solvation parameters for the corresponding types of atoms. [3]
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